Engineering allosteric protein switches by domain insertion | Zendy

Marc Ostermeier | Zendy

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Engineering allosteric protein switches by domain insertion

Author(s) -

Marc Ostermeier

Publication year - 2005

Publication title -

protein engineering design and selection

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.627

H-Index - 109

eISSN - 1741-0134

pISSN - 1741-0126

DOI - 10.1093/protein/gzi048

Subject(s) - allosteric regulation , domain (mathematical analysis) , permutation (music) , function (biology) , signal (programming language) , molecular switch , computer science , protein engineering , protein domain , computational biology , directed evolution , biophysics , biology , chemistry , physics , genetics , biochemistry , molecule , mathematics , gene , receptor , mathematical analysis , organic chemistry , enzyme , acoustics , programming language , mutant

Domain insertion is proving to be an effective way to construct hybrid proteins exhibiting switch-like behavior. In this strategy, two existing domains, the first exhibiting a signal recognition function and the second containing the function to be modulated, are fused such that the recognition of the signal by the first domain is transmitted to the second domain, thereby modulating its activity. Recent directed evolution experiments indicate that the structural space comprised of the recombination of unrelated protein domains may be rich in switching behavior, particularly when the circular permutation of domains is also employed. This bodes well for potential basic science, sensing and therapeutic applications of molecular switches.

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